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RALBP1 Antibody (Center) Blocking peptide

Synthetic peptide

     
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Product Information
Primary Accession Q15311
Clone Names 101008019
Peptide ID 101008019
Additional Information
Other Names RalA-binding protein 1, RalBP1, 76 kDa Ral-interacting protein, Dinitrophenyl S-glutathione ATPase, DNP-SG ATPase, Ral-interacting protein 1, RALBP1, RLIP1, RLIP76
Format Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name RALBP1
Synonyms RLIP1, RLIP76
Function Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin.
Cellular Location Membrane; Peripheral membrane protein
Tissue Location Expressed ubiquitously but at low levels. Shows a strong expression in the erythrocytes EMBL; L42542; AAB00103.1; -; mRNA EMBL; CH471113; EAX01601.1; -; Genomic_DNA EMBL; CH471113; EAX01602.1; -; Genomic_DNA EMBL; CH471113; EAX01604.1; -; Genomic_DNA EMBL; CH471113; EAX01605.1; -; Genomic_DNA EMBL; BC013126; AAH13126.1; -; mRNA CCDS; CCDS11845.1; - PIR; F59435; F59435 RefSeq; NP_006779.1; NM_006788.3 UniGene; Hs.528993; - PDB; 2KWH; NMR; -; A=393-446 PDB; 2KWI; NMR; -; B=393-446 PDB; 2MBG; NMR; -; A=184-446 PDBsum; 2KWH; - PDBsum; 2KWI; - PDBsum; 2MBG; - ProteinModelPortal; Q15311; - SMR; Q15311; - BioGrid; 116131; 88 CORUM; Q15311; - IntAct; Q15311; 57 MINT; Q15311; - STRING; 9606.ENSP00000019317; - DrugBank; DB00564; Carbamazepine DrugBank; DB00997; Doxorubicin DrugBank; DB00398; Sorafenib DrugBank; DB00541; Vincristine TCDB; 9.A.1.1.1; the non abc multidrug exporter (n-mde) family iPTMnet; Q15311; - PhosphoSitePlus; Q15311; - BioMuta; RALBP1; - DMDM; 34098413; - EPD; Q15311; - MaxQB; Q15311; - PaxDb; Q15311; - PeptideAtlas; Q15311; - PRIDE; Q15311; - ProteomicsDB; 60526; - DNASU; 10928; - Ensembl; ENST00000019317; ENSP00000019317; ENSG00000017797 Ensembl; ENST00000383432; ENSP00000372924; ENSG00000017797 GeneID; 10928; - KEGG; hsa:10928; - UCSC; uc002kob.4; human CTD; 10928; - DisGeNET; 10928; - EuPathDB; HostDB:ENSG00000017797.11; - GeneCards; RALBP1; - HGNC; HGNC:9841; RALBP1 HPA; CAB046010; - HPA; HPA046651; - MIM; 605801; gene neXtProt; NX_Q15311; - OpenTargets; ENSG00000017797; - PharmGKB; PA34199; - eggNOG; KOG4370; Eukaryota eggNOG; ENOG410XRJ9; LUCA GeneTree; ENSGT00920000148941; - HOGENOM; HOG000007929; - HOVERGEN; HBG044496; - InParanoid; Q15311; - KO; K08773; - OMA; LMHYKRL; - OrthoDB; EOG091G01CT; - PhylomeDB; Q15311; - TreeFam; TF315411; - Reactome; R-HSA-194840; Rho GTPase cycle SignaLink; Q15311; - ChiTaRS; RALBP1; human EvolutionaryTrace; Q15311; - GeneWiki; RALBP1; - GenomeRNAi; 10928; - PRO; PR:Q15311; - Proteomes; UP000005640; Chromosome 18 Bgee; ENSG00000017797; - CleanEx; HS_RALBP1; - ExpressionAtlas; Q15311; baseline and differential Genevisible; Q15311; HS GO; GO:0005829; C:cytosol; TAS:Reactome GO; GO:0016020; C:membrane; IDA:UniProtKB GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IDA:UniProtKB GO; GO:0015238; F:drug transmembrane transporter activity; IDA:UniProtKB GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB GO; GO:0048365; F:Rac GTPase binding; IPI:UniProtKB GO; GO:0017160; F:Ral GTPase binding; IPI:UniProtKB GO; GO:0022857; F:transmembrane transporter activity; IDA:UniProtKB GO; GO:0006935; P:chemotaxis; TAS:ProtInc GO; GO:1900753; P:doxorubicin transport; IDA:UniProtKB GO; GO:0006855; P:drug transmembrane transport; IDA:UniProtKB GO; GO:0006897; P:endocytosis; IBA:GO_Central GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome GO; GO:0007165; P:signal transduction; TAS:ProtInc GO; GO:0007264; P:small GTPase mediated signal transduction; IPI:UniProtKB GO; GO:0055085; P:transmembrane transport; IDA:UniProtKB Gene3D; 1.10.555.10; -; 1 InterPro; IPR008936; Rho_GTPase_activation_prot InterPro; IPR000198; RhoGAP_dom Pfam; PF00620; RhoGAP; 1 SMART; SM00324; RhoGAP; 1 SUPFAM; SSF48350; SSF48350; 1 PROSITE; PS50238; RHOGAP; 1 1: Evidence at protein level; 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; GTPase activation; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Transport INIT_MET 1 1 Removed. CHAIN 2 655 RalA-binding protein 1 /FTId=PRO_0000056733 DOMAIN 192 380 Rho-GAP. {ECO:0000255|PROSITE- ProRule:PRU00172} REGION 403 499 Interaction with RalA COMPBIAS 164 171 Poly-Lys MOD_RES 2 2 N-acetylthreonine MOD_RES 29 29 Phosphoserine MOD_RES 30 30 Phosphoserine MOD_RES 34 34 Phosphoserine MOD_RES 44 44 Phosphothreonine MOD_RES 48 48 Phosphoserine MOD_RES 62 62 Phosphoserine MOD_RES 92 92 Phosphoserine MOD_RES 93 93 Phosphoserine MOD_RES 461 461 Phosphoserine MOD_RES 463 463 Phosphoserine MOD_RES 645 645 Phosphoserine VARIANT 617 617 A -> V (in dbSNP:rs35867116) /FTId=VAR_049147 STRAND 184 187 {ECO:0000244|PDB:2MBG} HELIX 194 200 {ECO:0000244|PDB:2MBG} HELIX 211 222 {ECO:0000244|PDB:2MBG} TURN 223 225 {ECO:0000244|PDB:2MBG} TURN 228 232 {ECO:0000244|PDB:2MBG} HELIX 237 248 {ECO:0000244|PDB:2MBG} HELIX 255 257 {ECO:0000244|PDB:2MBG} HELIX 260 273 {ECO:0000244|PDB:2MBG} HELIX 280 291 {ECO:0000244|PDB:2MBG} HELIX 296 309 {ECO:0000244|PDB:2MBG} HELIX 312 334 {ECO:0000244|PDB:2MBG} HELIX 339 350 {ECO:0000244|PDB:2MBG} HELIX 354 367 {ECO:0000244|PDB:2MBG} STRAND 384 386 {ECO:0000244|PDB:2MBG} HELIX 395 414 {ECO:0000244|PDB:2KWH} TURN 417 419 {ECO:0000244|PDB:2MBG} HELIX 424 444 {ECO:0000244|PDB:2KWH} SEQUENCE 655 AA; 76063 MW; EC6F75329FD8D062 CRC64; MTECFLPPTS SPSEHRRVEH GSGLTRTPSS EEISPTKFPG LYRTGEPSPP HDILHEPPDV VSDDEKDHGK KKGKFKKKEK RTEGYAAFQE DSSGDEAESP SKMKRSKGIH VFKKPSFSKK KEKDFKIKEK PKEEKHKEEK HKEEKHKEKK SKDLTAADVV KQWKEKKKKK KPIQEPEVPQ IDVPNLKPIF GIPLADAVER TMMYDGIRLP AVFRECIDYV EKYGMKCEGI YRVSGIKSKV DELKAAYDRE ESTNLEDYEP NTVASLLKQY LRDLPENLLT KELMPRFEEA CGRTTETEKV QEFQRLLKEL PECNYLLISW LIVHMDHVIA KELETKMNIQ NISIVLSPTV QISNRVLYVF FTHVQELFGN VVLKQVMKPL RWSNMATMPT LPETQAGIKE EIRRQEFLLN CLHRDLQGGI KDLSKEERLW EVQRILTALK RKLREAKRQE CETKIAQEIA SLSKEDVSKE EMNENEEVIN ILLAQENEIL TEQEELLAME QFLRRQIASE KEEIERLRAE IAEIQSRQQH GRSETEEYSS ESESESEDEE ELQIILEDLQ RQNEELEIKN NHLNQAIHEE REAIIELRVQ LRLLQMQRAK AEQQAQEDEE PEWRGGAVQP PRDGVLEPKA AKEQPKAGKE PAKPSPSRDR KETSI
Research Areas
Citations (0)

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Background

RALBP1 plays a role in receptor-mediated endocytosis andis a downstream effector of the small GTP-binding protein RAL (seeRALA; MIM 179550). Small G proteins, such as RAL, have GDP-boundinactive and GTP-bound active forms, which shift from the inactiveto the active state through the action of RALGDS (MIM 601619),which in turn is activated by RAS (see HRAS; MIM 190020) (summaryby Feig, 2003 [PubMed 12888294]).

References

Singhal, S.S., et al. Int. J. Cancer 126(6):1327-1338(2010)Singhal, S.S., et al. Cancer Lett. 283(2):152-158(2009)Awasthi, Y.C., et al. J Toxicol Environ Health B Crit Rev 12(7):540-551(2009)Singhal, S.S., et al. Cancer Res. 69(10):4244-4251(2009)Singhal, S.S., et al. Biochem. Pharmacol. 77(6):1074-1083(2009)

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Cat# BP12329c
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